Conformational flexibility tunes the propensity of transthyretin to form fibrils through non-native intermediate states

Angewandte Chemie - International Edition

Volumn 53, Issue 47, 2014, Pages 12781-12784

  Das, Jitendra K ^a   Mall, Shyam S ^a   Bej, Aritra ^a   Mukherjee, Sujoy ^a  

^a INDIAN INSTITUTE OF CHEMICAL BIOLOGY   (India)

Author keywords

Amyloids; misfolding intermediates; NMR spectroscopy; protein folding; transthyretin

Indexed keywords

DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN FOLDING; PROTEINS;

AMYLOIDS; CONFORMATIONAL FLEXIBILITY; INTERMEDIATE STATE; MISFOLDING; PROTEIN AGGREGATION; RELAXATION DISPERSION; THERAPEUTIC STRATEGY; TRANSTHYRETIN;

DISEASES;

AMYLOID; PREALBUMIN;

CHEMISTRY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; SYNTHESIS;

AMYLOID; MOLECULAR DYNAMICS SIMULATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PREALBUMIN; PROTEIN CONFORMATION;

EID: 84911361093     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201407323     Document Type: Article

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